Evidence map›Paper›PMID 26943617›Full record

ArticleeLife2016

The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins.

Beth M Stadtmueller, Kathryn E Huey-Tubman, Carlos J López, Zhongyu Yang, Wayne L Hubbell, Pamela J Bjorkman

Open access · goldAbstract readComparative Study
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.3field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Veterinary sciences · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Tethering of soluble immune effectors to mucin and chitin reflects a convergent and dynamic role in gut immunity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Structural basis for Fc receptor recognition of immunoglobulin M.Nature structural & molecular biology · 2023
    Article
  17. Review
  18. Review
  19. Functional assays to evaluate antibody-mediated responses againstFrontiers in cellular and infection microbiology · 2023
    Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Beth M StadtmuellerDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Kathryn E Huey-TubmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Carlos J LópezJules Stein Eye Institute, University of California, Los Angeles, United States.
Zhongyu YangJules Stein Eye Institute, University of California, Los Angeles, United States.
Wayne L HubbellJules Stein Eye Institute, University of California, Los Angeles, United States.
Pamela J BjorkmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID http://orcid.org/0000-0002-2277-3990
California Institute of Technology · USUniversity of California, Los Angeles · US

Funding

Vision Research Core at UCLAP30EY000331 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Xian-Jie Yang · 1985 to 2026
$16.8M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
NEONATAL FC RECEPTOR/IGG INTERACTIONR01AI041239 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 1997 to 2018
$2.3M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR37EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1990 to 1999
–
NEI NIH HHS P30 EY000331NEI NIH HHS R01 EY005216NEI NIH HHS R37 EY005216NIAID NIH HHS R01 AI041239
6 · The paper itself

Abstract

As a first-line vertebrate immune defense, the polymeric immunoglobulin receptor (pIgR) transports polymeric IgA and IgM across epithelia to mucosal secretions, where the cleaved ectodomain (secretory component; SC) becomes a component of secretory antibodies, or when unliganded, binds and excludes bacteria. Here we report the 2.6Å crystal structure of unliganded human SC (hSC) and comparisons with a 1.7Å structure of teleost fish SC (tSC), an early pIgR ancestor. The hSC structure comprises five immunoglobulin-like domains (D1-D5) arranged as a triangle, with an interface between ligand-binding domains D1 and D5. Electron paramagnetic resonance measurements confirmed the D1-D5 interface in solution and revealed that it breaks upon ligand binding. Together with binding studies of mutant and chimeric SCs, which revealed domain contributions to secretory antibody formation, these results provide detailed models for SC structure, address pIgR evolution, and demonstrate that SC uses multiple conformations to protect mammals from pathogens.

Indexed as

AnimalsCrystallography, X-RayElectron Spin Resonance SpectroscopyFishesHumansImmunoglobulinsModels, MolecularProtein ConformationProtein Structure, TertiarySecretory ComponentImmunoglobulinsSecretory Componentbiophysicscrystal structuresdouble electron-electron resonancehumanimmunologypolymeric ig receptor (pIgR)secretory component (SC)secretory igA/igMstructural biologysurface plasmon resonance

Identifiers

PMID26943617
PMCPMC4786434
OpenAlexW2291829437

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.